Gene Ontology annotation based on Enzyme Commission mapping
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Structures of two bacterial resistance factors mediating tRNA-dependent aminoacylation of phosphatidylglycerol with lysine or alanine.
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Crystal structure of the P. aeruginosa A-PGS catalytic domain, with a tunnel admitting PG and aminoacyl-tRNA from opposite sides; substrate determinants defined biochemically.
"Both proteins reveal a continuous tunnel that allows the hydrophobic lipid substrate PG and the polar aminoacyl-tRNA substrate to access the catalytic site from opposite directions."
Adaptation of Pseudomonas aeruginosa to various conditions includes tRNA-dependent formation of alanyl-phosphatidylglycerol.
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PA0920 is the A-PG synthase; the deletion makes no A-PG, expression in E. coli confers A-PG, and the partially purified enzyme is tRNA(Ala)-dependent and in the inner membrane.
"Consequently, the protein encoded by PA0920 was named A-PG synthase."
Alanyl-phosphatidylglycerol synthase: mechanism of substrate recognition during tRNA-dependent lipid modification in Pseudomonas aeruginosa.
Resistance phenotypes mediated by aminoacyl-phosphatidylglycerol synthases.
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P. aeruginosa naturally makes A-PG, not L-PG; aaPGS specificity is not marked by a sequence motif.
"the specificity of an individual enzyme is not reflected in terms of a characteristic sequence motif"
Identification and characterization of a periplasmic aminoacyl-phosphatidylglycerol hydrolase responsible for Pseudomonas aeruginosa lipid homeostasis.
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The A-PG hydrolase PA0919 controls A-PG levels; lipid homeostasis is attributed to PA0919.
"Analysis of the polar lipid content of the deletion mutant ΔPA0919 indicated significantly enlarged levels of alanyl-PG."